This project will continue to emphasize the application of spectrofluorometric methods and fluorescence microscopy to the analysis of protein conformation, protein-small molecule interactions, protein- protein interactions, and the interaction of proteins within supramolecular assemblies. These methods depend on the enhanced fluorescence of certain compounds when they are bound to apolar regions of protein molecules and on the ability to label proteins with fluorescent molecules without significantly altering their activity. We will continue to study the use of these approaches in zymogen activations, allosteric changes, and interactions on membrane structures. We are also studying the structure and function of immunoglobulins, lectins, and hemagglutinins partly as examples for exploration of the use of fluorescence spectroscopy and fluorescence microscopy in protein chemistry.